Skip Header

Contribute Send feedback
Read comments (?) or add your own

P25374 (NFS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine desulfurase, mitochondrial
EC=2.8.1.7
Alternative name(s):
tRNA-splicing protein SPL1
Gene names
Name:NFS1
Synonyms:SPL1
Ordered Locus Names:YCL017C
ORF Names:YCL17C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Involved in both tRNA-processing and mitochondrial metabolism.

Catalytic activity

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.

Cofactor

Pyridoxal phosphate By similarity.

Subcellular location

Mitochondrion.

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ISD11Q6Q5602EBI-11991,EBI-784315
ISU1Q030202EBI-11991,EBI-29901

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Potential
Chain34 – 497464Cysteine desulfurase, mitochondrial
PRO_0000001304

Sites

Active site4211 By similarity

Amino acid modifications

Modified residue2991N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict1501H → Y in AAA34814. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25374 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: D709E326B3921BCC

FASTA49754,467
        10         20         30         40         50         60 
MLKSTATRSI TRLSQVYNVP AATYRACLVS RRFYSPPAAG VKLDDNFSLE THTDIQAAAK 

        70         80         90        100        110        120 
AQASARASAS GTTPDAVVAS GSTAMSHAYQ ENTGFGTRPI YLDMQATTPT DPRVLDTMLK 

       130        140        150        160        170        180 
FYTGLYGNPH SNTHSYGWET NTAVENARAH VAKMINADPK EIIFTSGATE SNNMVLKGVP 

       190        200        210        220        230        240 
RFYKKTKKHI ITTRTEHKCV LEAARAMMKE GFEVTFLNVD DQGLIDLKEL EDAIRPDTCL 

       250        260        270        280        290        300 
VSVMAVNNEI GVIQPIKEIG AICRKNKIYF HTDAAQAYGK IHIDVNEMNI DLLSISSHKI 

       310        320        330        340        350        360 
YGPKGIGAIY VRRRPRVRLE PLLSGGGQER GLRSGTLAPP LVAGFGEAAR LMKKEFDNDQ 

       370        380        390        400        410        420 
AHIKRLSDKL VKGLLSAEHT TLNGSPDHRY PGCVNVSFAY VEGESLLMAL RDIALSSGSA 

       430        440        450        460        470        480 
CTSASLEPSY VLHALGKDDA LAHSSIRFGI GRFSTEEEVD YVVKAVSDRV KFLRELSPLW 

       490 
EMVQEGIDLN SIKWSGH

« Hide

References

« Hide 'large scale' references
[1]"SPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing."
Leong-Morgenthaler P.M., Kolman C., Oliver S.G., Hottinger H., Soell D.
J. Bacteriol. 175:1433-1442(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 150.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Nucleotide sequence of the 3' terminal region of the LEU2 gene from Saccharomyces cerevisiae."
Froman B.E., Tait R.C., Rodriguez R.L.
Gene 31:257-261(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-497.
[6]"The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins."
Kispal G., Csere P., Prohl C., Lill R.
EMBO J. 18:3981-3989(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution."
Li J., Kogan M., Knight S.A., Pain D., Dancis A.
J. Biol. Chem. 274:33025-33034(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M98808 Genomic DNA. Translation: AAA34814.1.
X59720 Genomic DNA. Translation: CAA42344.2.
M12909 Genomic DNA. Translation: AAA66918.1.
BK006937 Genomic DNA. Translation: DAA07466.1.
PIRS19343.
RefSeqNP_009912.2. NM_001178664.1.

3D structure databases

ProteinModelPortalP25374.
SMRP25374. Positions 99-491.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2948N.
IntActP25374. 12 interactions.
MINTMINT-474525.
STRING4932.YCL017C.

Proteomic databases

PaxDbP25374.
PeptideAtlasP25374.
PRIDEP25374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL017C; YCL017C; YCL017C.
GeneID850343.
KEGGsce:YCL017C.

Organism-specific databases

CYGDYCL017c.
SGDS000000522. NFS1.

Phylogenomic databases

eggNOGCOG1104.
GeneTreeENSGT00530000063513.
HOGENOMHOG000017510.
KOK04487.
OMALWEMFKQ.
OrthoDBEOG4643M5.

Gene expression databases

GenevestigatorP25374.
GermOnlineYCL017C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR010240. Cys_deSase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR02006. IscS. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965791.

Entry information

Entry nameNFS1_YEAST
AccessionPrimary (citable) accession number: P25374
Secondary accession number(s): D6VQZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 15, 2004
Last modified: May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents